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HEADER HYDROLASE 19-OCT-12 3W06
TITLE CRYSTAL STRUCTURE OF ARABIDOPSIS THALIANA DWARF14 LIKE (ATD14L)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE, ALPHA/BETA FOLD FAMILY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PUTATIVE UNCHARACTERIZED PROTEIN AT4G37470, PUTATIVE
COMPND 5 UNCHARACTERIZED PROTEIN AT4G37470, PUTATIVE UNCHARACTERIZED PROTEIN
COMPND 6 F6G17.120;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: AT4G37470, F6G17.120;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET49B
KEYWDS KARRIKIN SIGNALING, ALPHA/BETA HYDROLASE, KARRIKIN BINDING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KAGIYAMA,Y.HIRANO,T.MORI,S.Y.KIM,J.KYOZUKA,Y.SETO,S.YAMAGUCHI,
AUTHOR 2 T.HAKOSHIMA
REVDAT 1 23-JAN-13 3W06 0
JRNL AUTH M.KAGIYAMA,Y.HIRANO,T.MORI,S.Y.KIM,J.KYOZUKA,Y.SETO,
JRNL AUTH 2 S.YAMAGUCHI,T.HAKOSHIMA
JRNL TITL STRUCTURES OF D14 AND D14L IN THE STRIGOLACTONE AND KARRIKIN
JRNL TITL 2 SIGNALING PATHWAYS.
JRNL REF GENES CELLS 2013
JRNL REFN ESSN 1365-2443
JRNL PMID 23301669
JRNL DOI 10.1111/GTC.12025
REMARK 2
REMARK 2 RESOLUTION. 1.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 86188
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.133
REMARK 3 R VALUE (WORKING SET) : 0.132
REMARK 3 FREE R VALUE : 0.162
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4538
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6117
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.1950
REMARK 3 BIN FREE R VALUE SET COUNT : 312
REMARK 3 BIN FREE R VALUE : 0.2390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2070
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 304
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : 0.10000
REMARK 3 B33 (A**2) : -0.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.032
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.034
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.020
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.942
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2401 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3297 ; 1.639 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 324 ; 5.995 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 112 ;35.376 ;24.464
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 394 ;12.430 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;14.474 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 373 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1890 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1486 ; 2.851 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2452 ; 4.023 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 915 ; 6.304 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 834 ; 8.614 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2401 ; 3.393 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3W06 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-OCT-12.
REMARK 100 THE RCSB ID CODE IS RCSB095719.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAY-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90
REMARK 200 MONOCHROMATOR : ROTATED-INCLINED DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR , SI (111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90920
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.53500
REMARK 200 FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3W04
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M AMMONIUM SULFATE, 0.2M BICINE, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 27.80150
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -1
REMARK 465 PRO A 0
REMARK 465 MET A 1
REMARK 465 ALA A 269
REMARK 465 MET A 270
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 17 CG CD OE1 OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 176 CA
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NZ LYS A 11 O HOH A 685 1.65
REMARK 500 CE MET A 198 C1 EDO A 305 1.76
REMARK 500 NH2 ARG A 176 O HOH A 678 1.92
REMARK 500 OE2 GLU A 5 O HOH A 700 2.05
REMARK 500 NE2 GLN A 213 OG SER A 225 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 564 O HOH A 664 2455 1.72
REMARK 500 CE1 PHE A 75 O HOH A 633 2444 2.00
REMARK 500 CZ PHE A 75 O HOH A 645 2444 2.09
REMARK 500 CZ PHE A 75 O HOH A 633 2444 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 28 -164.85 -120.05
REMARK 500 SER A 95 -125.21 55.97
REMARK 500 ARG A 123 123.91 -171.27
REMARK 500 ASN A 149 98.51 -161.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 306
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3W04 RELATED DB: PDB
REMARK 900 RELATED ID: 3W05 RELATED DB: PDB
DBREF 3W06 A 1 270 UNP Q9SZU7 Q9SZU7_ARATH 1 270
SEQADV 3W06 GLY A -1 UNP Q9SZU7 EXPRESSION TAG
SEQADV 3W06 PRO A 0 UNP Q9SZU7 EXPRESSION TAG
SEQRES 1 A 272 GLY PRO MET GLY VAL VAL GLU GLU ALA HIS ASN VAL LYS
SEQRES 2 A 272 VAL ILE GLY SER GLY GLU ALA THR ILE VAL LEU GLY HIS
SEQRES 3 A 272 GLY PHE GLY THR ASP GLN SER VAL TRP LYS HIS LEU VAL
SEQRES 4 A 272 PRO HIS LEU VAL ASP ASP TYR ARG VAL VAL LEU TYR ASP
SEQRES 5 A 272 ASN MET GLY ALA GLY THR THR ASN PRO ASP TYR PHE ASP
SEQRES 6 A 272 PHE ASP ARG TYR SER ASN LEU GLU GLY TYR SER PHE ASP
SEQRES 7 A 272 LEU ILE ALA ILE LEU GLU ASP LEU LYS ILE GLU SER CYS
SEQRES 8 A 272 ILE PHE VAL GLY HIS SER VAL SER ALA MET ILE GLY VAL
SEQRES 9 A 272 LEU ALA SER LEU ASN ARG PRO ASP LEU PHE SER LYS ILE
SEQRES 10 A 272 VAL MET ILE SER ALA SER PRO ARG TYR VAL ASN ASP VAL
SEQRES 11 A 272 ASP TYR GLN GLY GLY PHE GLU GLN GLU ASP LEU ASN GLN
SEQRES 12 A 272 LEU PHE GLU ALA ILE ARG SER ASN TYR LYS ALA TRP CYS
SEQRES 13 A 272 LEU GLY PHE ALA PRO LEU ALA VAL GLY GLY ASP MET ASP
SEQRES 14 A 272 SER ILE ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN
SEQRES 15 A 272 MET ARG PRO ASP ILE ALA LEU SER VAL GLY GLN THR ILE
SEQRES 16 A 272 PHE GLN SER ASP MET ARG GLN ILE LEU PRO PHE VAL THR
SEQRES 17 A 272 VAL PRO CYS HIS ILE LEU GLN SER VAL LYS ASP LEU ALA
SEQRES 18 A 272 VAL PRO VAL VAL VAL SER GLU TYR LEU HIS ALA ASN LEU
SEQRES 19 A 272 GLY CYS GLU SER VAL VAL GLU VAL ILE PRO SER ASP GLY
SEQRES 20 A 272 HIS LEU PRO GLN LEU SER SER PRO ASP SER VAL ILE PRO
SEQRES 21 A 272 VAL ILE LEU ARG HIS ILE ARG ASN ASP ILE ALA MET
HET EDO A 301 4
HET EDO A 302 4
HET EDO A 303 4
HET EDO A 304 4
HET EDO A 305 4
HET EDO A 306 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 6(C2 H6 O2)
FORMUL 8 HOH *304(H2 O)
HELIX 1 1 GLY A 2 HIS A 8 1 7
HELIX 2 2 ASP A 29 LYS A 34 5 6
HELIX 3 3 LEU A 36 LEU A 40 5 5
HELIX 4 4 ASN A 58 PHE A 62 5 5
HELIX 5 5 ASP A 65 SER A 68 5 4
HELIX 6 6 ASN A 69 LEU A 84 1 16
HELIX 7 7 SER A 95 ARG A 108 1 14
HELIX 8 8 GLU A 135 ASN A 149 1 15
HELIX 9 9 ASN A 149 GLY A 163 1 15
HELIX 10 10 SER A 168 MET A 181 1 14
HELIX 11 11 ARG A 182 GLN A 195 1 14
HELIX 12 12 MET A 198 VAL A 205 5 8
HELIX 13 13 PRO A 221 LEU A 232 1 12
HELIX 14 14 LEU A 247 SER A 252 1 6
HELIX 15 15 SER A 252 ASN A 266 1 15
SHEET 1 A 7 LYS A 11 ILE A 13 0
SHEET 2 A 7 ARG A 45 LEU A 48 -1 O LEU A 48 N LYS A 11
SHEET 3 A 7 THR A 19 GLY A 23 1 N ILE A 20 O VAL A 47
SHEET 4 A 7 CYS A 89 HIS A 94 1 O HIS A 94 N GLY A 23
SHEET 5 A 7 PHE A 112 ILE A 118 1 O VAL A 116 N PHE A 91
SHEET 6 A 7 CYS A 209 LYS A 216 1 O HIS A 210 N MET A 117
SHEET 7 A 7 SER A 236 ASP A 244 1 O VAL A 237 N ILE A 211
SITE 1 AC1 6 GLN A 131 GLY A 133 PRO A 221 HOH A 497
SITE 2 AC1 6 HOH A 500 HOH A 695
SITE 1 AC2 4 HIS A 210 HIS A 263 ASN A 266 HOH A 697
SITE 1 AC3 4 LYS A 34 VAL A 37 HOH A 492 HOH A 698
SITE 1 AC4 3 HIS A 39 ARG A 265 HOH A 572
SITE 1 AC5 6 ASN A 69 LEU A 70 SER A 196 ASP A 197
SITE 2 AC5 6 MET A 198 HOH A 541
SITE 1 AC6 4 GLU A 82 LYS A 85 HOH A 546 HOH A 584
CRYST1 50.953 55.603 53.128 90.00 115.81 90.00 P 1 21 1 2
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019626 0.000000 0.009492 0.00000
SCALE2 0.000000 0.017985 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020908 0.00000
TER 2307 ILE A 268
MASTER 336 0 6 15 7 0 8 6 2398 1 24 21
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